Phosphatidylethanolamine made in the inner mitochondrial membrane is essential for yeast cytochrome bc 1 complex function
| Autor: | J. Michael McCaffery, Steven M. Claypool, Arnab Modak, Chunyan Wang, Elizabeth Calzada, Erica Avery, Pingdewinde N. Sam, Xianlin Han, Nathan N. Alder |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Cytochrome Protein subunit Science General Physics and Astronomy 02 engineering and technology Mitochondrion General Biochemistry Genetics and Molecular Biology 03 medical and health sciences chemistry.chemical_compound Endomembrane system Inner mitochondrial membrane lcsh:Science Phosphatidylethanolamine Multidisciplinary biology Chemistry General Chemistry 021001 nanoscience & nanotechnology Cell biology 030104 developmental biology Coenzyme Q – cytochrome c reductase biology.protein lcsh:Q 0210 nano-technology Phosphatidylserine decarboxylase |
| Zdroj: | Nature Communications, Vol 10, Iss 1, Pp 1-17 (2019) |
| ISSN: | 2041-1723 |
| Popis: | Of the four separate PE biosynthetic pathways in eukaryotes, one occurs in the mitochondrial inner membrane (IM) and is executed by phosphatidylserine decarboxylase (Psd1). Deletion of Psd1 is lethal in mice and compromises mitochondrial function. We hypothesize that this reflects inefficient import of non-mitochondrial PE into the IM. Here, we test this by re-wiring PE metabolism in yeast by re-directing Psd1 to the outer mitochondrial membrane or the endomembrane system and show that PE can cross the IMS in both directions. Nonetheless, PE synthesis in the IM is critical for cytochrome bc1 complex (III) function and mutations predicted to disrupt a conserved PE-binding site in the complex III subunit, Qcr7, impair complex III activity similar to PSD1 deletion. Collectively, these data challenge the current dogma of PE trafficking and demonstrate that PE made in the IM by Psd1 support the intrinsic functionality of complex III. Phosphatidylethanolamine (PE) is synthesized by four separate pathways, although surprisingly, perturbing mitochondrial PE synthesis compromises mitochondrial function. Here, the authors show that mitochondrial PE synthesis is required for Complex III function and challenge PE trafficking dogma. |
| Databáze: | OpenAIRE |
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